IAI Accepts, published online ahead of print on 26 October 2009

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Infect. Immun. doi:10.1128/IAI.00776-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Major Surface Protease (MSP, or GP63) of Trypanosomatids, One Size Fits All?

Chaoqun Yao^*

Department of Veterinary Sciences and Wyoming State Veterinary Laboratory, University of Wyoming, Laramie, WY 82070

^* To whom correspondence should be addressed. Email: cyao{at}uwyo.edu.

Major surface protease (MSP, or GP63) is the most abundant glycoprotein localized to the plasma membrane of Leishmania promastigotes. It plays several important roles in the pathogenesis of leishmaniasis. These include, but are not limited to: 1) evading complement-mediated lysis, 2) facilitating macrophage (Mø) phagocytosis of promastigotes, 3) interacting with extracellular matrix, 4) inhibiting natural killer cellular functions, 5) resisting to antimicrobial peptide killing, 6) degrading cytosolic proteins of Mø and fibroblasts, and 7) promoting survival of the intracellular amastigotes in Mø. MSP homologues have been found in all other trypanosomatids studied to date including heteroxenous members of Trypanosoma cruzi, the extracellular T. brucei, unusual intraerythrocytic Endotrypanum spp., and phytoparasitic Phytomonas spp. and numerous monoxenous species. They very likely perform different roles than those in Leishmania spp. Multiple MSPs in individual cells may play distinct roles at some time points and collaborative roles at the others in trypanosomatid life cycles; they may play redundant roles at most time. The cellular locations and the extracellular release of MSPs are also discussed in connection with MSP functions in leishmanial promastigotes.